Premium
[P1–231]: A CROSS‐SECTIONAL STUDY OF SERUM BRAIN DERIVED NEUROTROPIC FACTOR (BDNF) CONCENTRATIONS IN A SAUDI POPULATION AND ALZHEIMER's DISEASE
Author(s) -
Alsabhan Jawza Fahad,
Gard Paul,
Scutt Greg,
Abanmy Norah
Publication year - 2017
Publication title -
alzheimer's and dementia
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 6.713
H-Index - 118
eISSN - 1552-5279
pISSN - 1552-5260
DOI - 10.1016/j.jalz.2017.06.051
Subject(s) - dementia , brain derived neurotrophic factor , clinical dementia rating , neurotrophic factors , medicine , alzheimer's disease , population , cognitive decline , neurotrophin , psychology , disease , cross sectional study , oncology , endocrinology , pathology , receptor , environmental health
(APP) containing vesicles in neuron. Kinesin-1 is a tetrameric protein composed of two heavy chains (KHCs) and two light chains (KLCs). The tetratricopeptide repeat (TPR) domain of KLC1 may be responsible for binding APP either directly or via interaction with C-jun N-terminal kinase-interacting protein 1 (JIP1). However, the binding partners of the TPR domain of KLCs have not yet been fully identified. Methods: We were used the yeast two-hybrid system to identify the binding proteins that interact with the TPR domain of KLC1. The binding affinity was quantified by measuring b-galactosidase activity in liquid cultures of yeast transformed cells. Direct interaction between binding proteins and KLC1 in mammalian cells as well as in vitro was assayed using the co-immunoprecipitation with the antibodies. The cellular co-localization in cells was used the immunocytochemistry. Results: We revealed an interaction between the TPR domain of KLC1 anddynamin-1-like protein (Dnm1L), also known as dynamin-related protein 1. Dnm1L bound to the six TPR domain of KLC1 and did not interact with KIF5s. Dnm1L interacts with KLC1 through itsGTPase effector domain (GED) domain. When co-expressed in HEK-293T cells, co-localized with KLC1 and co-immunoprecipitated with KLC1, but not KIF5B. Conclusions:We suggest that, after mitochondrial fission, interaction of Dnm1L with KLC1 may lead to dissociation of kinesin-1 tetramer, allowing KIF5 to interact with milton and transport mitochondria.